1Jemal, A, Siegel, R, Ward, E, et al. (2009) Cancer statistics, 2009. Cancer J Clin 59, 225–249.
2Cummings, JH & Bingham, SA (1998) Fortnightly review – diet and the prevention of cancer. Br Med J 317, 1636–1640.
3Reddy, BS (2000) Novel approaches to the prevention of colon cancer by nutritional manipulation and chemoprevention. Cancer Epidemiol Biomark Prev 9, 239–247.
4MacFarlane, AJ & Stover, PJ (2007) Factors in gastrointestinal cancers: convergence of genetic, nutritional and inflammatory. Nutr Rev 65, S157–S166.
5Kennedy, AR, Billings, PC, Wan, XS, et al. (2002) Effects of Bowman–Birk inhibitor on rat colon carcinogenesis. Nutr Cancer 43, 174–186.
6Clemente, A & Domoney, C (2006) Biological significance of polymorphism in plant protease inhibitors from the Bowman–Birk class. Curr Prot Pept Sci 7, 201–216.
7Clemente, A & Domoney, C (2007) Therapeutic properties of legume protease inhibitors from the Bowman–Birk class. In Recent Progress in Medicinal Plants, pp. 397–417 [Govil, JN, Singh, VK and Sharma, RK, editors]. vol. 20, Houston, TX: Studium Press.
8Clemente, A, Sonnante, G & Domoney, C (2011) Bowman–Birk inhibitors from legumes and human gastrointestinal health: current status and perspectives. Curr Prot Pept Sci 12, 358–373.
9Chen, P, Rose, J, Love, R, et al. (1992) Reactive sites of an anticarcinogenic Bowman–Birk proteinase inhibitor are similar to other trypsin inhibitors. J Biol Chem 267, 1990–1994.
10Ramasarma, PR, Appu Rao, AG & Rao, DR (1995) Role of disulfide linkages in structure and activity of proteinase inhibitor from horsegram (Dolichos biflorus). Biochim Biophys Acta 1248, 35–42.
11Trivedi, MV, Laurence, JS & Siahann, TJ (2009) The role of thiols and disulfides on protein stability. Curr Prot Pept Sci 10, 614–625.
12Clemente, A, Jimenez, E, Marín-Manzano, MC, et al. (2008) Active Bowman–Birk inhibitors survive gastrointestinal digestion at the terminal ileum of pigs fed chickpea-based diets. J Sci Food Agric 88, 523–531.
13Marín-Manzano, MC, Ruiz, R, Jimenez, E, et al. (2009) Anti-carcinogenic soyabean Bowman–Birk inhibitors survive faecal fermentation in their active form and do not affect the microbiota composition in vitro. Br J Nutr 101, 967–971.
14Kennedy, AR, Szuhaj, BF, Newberne, PM, et al. (1993) Preparation and production of a cancer chemopreventive agent, Bowman–Birk inhibitor concentrate. Nutr Cancer 19, 281–302.
15Clemente, A, Moreno, J, Marín-Manzano, MC, et al. (2010) The cytotoxic effect of Bowman–Birk isoinhibitors from soybean on HT29 human colorectal cancer cells is related to their intrinsic ability to inhibit serine proteases. Mol Nutr Food Res 54, 396–405.
16Clemente, A, Gee, JM, Johnson, IT, et al. (2005) Pea (Pisum sativum L.) protease inhibitors from the Bowman–Birk class influence the growth of human colorectal adenocarcinoma HT29 cells in vitro. J Agric Food Chem 53, 8979–8986.
17Caccialupi, P, Ceci, LR, Siciliano, RA, et al. (2010) Bowman–Birk inhibitors in lentil: heterologous expression, functional characterisation and anti-proliferative properties in human colon cancer cells. Food Chem 120, 1058–1066.
18Domoney, C. (1999) Inhibitors of legume seeds. In Seed Proteins, pp. 635–655 [Shewry, PR and Casey, R, editors]. The Netherlands: Kluwer Academic Publishers.
19Domoney, C, Welham, T, Ellis, N, et al. (2002) Three classes of proteinase inhibitor gene have distinct but overlapping patterns of expression in Pisum sativum plants. Plant Mol Biol 48, 319–329.
20Ho, S, Hunt, H, Horton, R, et al. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51–59.
21Domoney, C & Welham, T (1992) Trypsin inhibitors in Pisum: variation in amount and pattern of accumulation in developing seed. Seed Sci Res 2, 147–154.
22Clemente, A, MacKenzie, DA, Jeenes, DJ, et al. (2004) The effect of variation within inhibitory domains on the activity of pea protease inhibitors from the Bowman–Birk class. Protein Express Purif 36, 106–114.
23Copeland, RA, Lombardo, D, Giannaras, J, et al. (1995) Estimating K i values for tight-binding inhibitors from dose-response plots. Bioorg Med Chem Lett 5, 1947–1952.
24Domoney, C, Welham, T, Sidebottom, C, et al. (1995) Multiple isoforms of Pisum trypsin inhibitors result from modification of two primary gene products. FEBS Lett 360, 15–20.
25Schechter, I & Berger, A (1967) On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27, 157–162.
26Damaso, MC, Almeida, MS, Kurtenbach, E, et al. (2003) Optimized expression of a thermostable xylanase from Thermomyces lanuginosus in Pichia pastoris. Appl Environ Microbiol 69, 6064–6072.
27Chen, Z, Wang, D, Cong, Y, et al. (2011) Recombinant antimicrobial peptide hPAB-β expressed in Pichia pastoris, a potential agent active against methicillin-resistant Staphylococcus aureus. Appl Microbiol Biotechnol 89, 281–291.
28Scarafoni, A, Consonni, A, Galbusera, V, et al. (2008) Identification and characterization of a Bowman–Birk inhibitor active towards trypsin but not chymotrypsin in Lupinus albus seeds. Phytochem 69, 1820–1825.
29Kennedy, AR (1998) Chemopreventive agents: protease inhibitors. Pharmacol Ther 78, 167–209.
30Kennedy, AR (1998) The Bowman–Birk inhibitor from soybeans as an anticarcinogenic agent. Am J Clin Nutr 68, 1406s–1412s.
31Singh, RR & Appu Rao, AG (2002) Reductive unfolding and oxidative refolding of a Bowman–Birk inhibitor from horsegram seeds (Dolichos biflorus): evidence for “hyperreactive” disulfide bonds and rate-limiting nature of disulfide isomerisation in folding. Biochim Biophys Acta 1597, 280–291.
32Volpicella, M, Ceci, LR, Cordewener, J, et al. (2003) Properties of purified gut trypsin from Helicoverpa zea, adapted to protease inhibitors. Eur J Biochem 270, 10–19.
33Yavelow, J, Collins, M, Birk, Y, et al. (1985) Nanomolar concentrations of Bowman–Birk soybean protease inhibitor suppress X-ray induced transformation in vitro. Proc Natl Acad Sci U S A 82, 5395–5399.